Capacitation suppression by mouse seminal vesicle autoantigen involves a decrease in plasma membrane Ca2+-ATPase (PMCA)-mediated intracellular calcium

Shing Hwa Lu, Yuan Kuei Yen, Thai Yen Ling, Kur Ta Cheng, Jye An Shu, Heng Kien Au, Yen Hua Huang

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)


Successful fertilization is tightly regulated by capacitation and decapacitation processes. Without appropriate decapacitation regulation, sperm would undergo a spontaneous acrosome reaction which leads to loss of fertilization ability. Seminal plasma is known to negatively regulate sperm capacitation. However, the suppressive mechanisms still remain unclear. In this study, we demonstrate the decapacitation mechanism of mouse seminal vesicle autoantigen (SVA) might target membrane sphingomyelin (SPM) and regulate plasma membrane Ca2+-ATPase (PMCA) activity. The SVA was shown to suppress sperm capacitation induced by a broad panel of capacitation factors (bovine serum albumin (BSA), PAF, and cyclodextrin (CD)). Furthermore, SVA significantly decreased [Ca2+]i and NaHCO3-induced [cAMP]i. Cyclic AMP agonists bypassed the SVA's suppressive ability. Importantly, the SVA may regulate PMCA activity which was evidenced by the fact that the SVA decreased the [Ca2+]i and intracellular pH (pHi) of sperm; meanwhile, a PMCA inhibitor (carboxyeosin) could reverse SVA's suppression of [Ca2+]i. The potential target of the SVA on membrane SPM/lipid rafts was highlighted by the high binding affinity of SPM-SVA (with a Kd of ∼3 μM) which was close to the IC50 of SVA's suppressive activity. Additionally, treatment of mink lung epithelial cells with the SVA enhanced plasminogen activator inhibitor (PAI)-1 expression stimulated by tumor growth factor (TGF)-β and CD. These observations supported the membrane lipid-raft targeting of SVA. In summary, in this paper, we demonstrate that the decapacitation mechanism of the SVA might target membrane sphingolipid SPM and regulate PMCA activity to lower [Ca 2+]i, thereby decreasing the [cAMP]i level and preventing sperm pre-capacitation.

Original languageEnglish
Pages (from-to)1188-1198
Number of pages11
JournalJournal of Cellular Biochemistry
Issue number5
Publication statusPublished - Dec 1 2010


  • cAMP
  • calcium
  • decapacitation
  • plasma membrane Ca-ATPase (PMCA)
  • protein tyrosine phosphorylation
  • seminal vesicle
  • sperm

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry
  • Cell Biology


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